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Conserved domains on  [gi|1720354836|ref|XP_030109045|]
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R3H domain-containing protein 1 isoform X17 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
38-89 1.46e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


:

Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 63.11  E-value: 1.46e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720354836  38 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 89
Cdd:pfam12752   3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
322-647 6.32e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 322 AASHMFSQPVGPLQSSSQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQFSHMSLARQPSADGSDPHATMFQSTVVLQSPQ 401
Cdd:pfam03154 162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 402 qsgyivtTAPPHPPPPPPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQYR 481
Cdd:pfam03154 242 -------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQVP 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 482 PIPSVHHSSHLNQPLPQPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQG 561
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQS 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 562 SQGIAHQTYQQPVVFPNQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPCS 630
Cdd:pfam03154 372 HKHPPHLSGPSPFQMNSNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPPA 444
                         330
                  ....*....|....*..
gi 1720354836 631 SQQLQGHQCAAVPQQPP 647
Cdd:pfam03154 445 ASHPPTSGLHQVPSQSP 461
 
Name Accession Description Interval E-value
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
38-89 1.46e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 63.11  E-value: 1.46e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720354836  38 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 89
Cdd:pfam12752   3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
322-647 6.32e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 322 AASHMFSQPVGPLQSSSQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQFSHMSLARQPSADGSDPHATMFQSTVVLQSPQ 401
Cdd:pfam03154 162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 402 qsgyivtTAPPHPPPPPPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQYR 481
Cdd:pfam03154 242 -------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQVP 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 482 PIPSVHHSSHLNQPLPQPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQG 561
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQS 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 562 SQGIAHQTYQQPVVFPNQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPCS 630
Cdd:pfam03154 372 HKHPPHLSGPSPFQMNSNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPPA 444
                         330
                  ....*....|....*..
gi 1720354836 631 SQQLQGHQCAAVPQQPP 647
Cdd:pfam03154 445 ASHPPTSGLHQVPSQSP 461
 
Name Accession Description Interval E-value
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
38-89 1.46e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 63.11  E-value: 1.46e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720354836  38 QKRYILKRDNSSFD--KDDSQMRIRLKDDRRSKSIEEREEEYQRARDRIFSQDS 89
Cdd:pfam12752   3 PKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
322-647 6.32e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 322 AASHMFSQPVGPLQSSSQPVQCSPAPYPSPLLPVSPTQQYSVDNLGAQFSHMSLARQPSADGSDPHATMFQSTVVLQSPQ 401
Cdd:pfam03154 162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 402 qsgyivtTAPPHPPPPPPPPPPPPSLPPGQSVPTASFSASGHPVSQPVLQQQGFLPQPSPQMPacycAPGHYHSSQPQYR 481
Cdd:pfam03154 242 -------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQVP 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 482 PIPSVHHSSHLNQPLPQPaqhtgyqvmPNQQQNYQGivgvQSPQSQSLMGGqPNSTgPHIQgvviPYPSVPSYQVSLPQG 561
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTP---------PSQSQLQSQ----QPPREQPLPPA-PLSM-PHIK----PPPTTPIPQLPNPQS 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354836 562 SQGIAHQTYQQPVVFPNQ-----------SNQGSLPTTGMPVYYSVIPPGQQSNLSSAvgylQHPGSEQVQfprTTSPCS 630
Cdd:pfam03154 372 HKHPPHLSGPSPFQMNSNlppppalkplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPA----QPPVLTQSQ---SLPPPA 444
                         330
                  ....*....|....*..
gi 1720354836 631 SQQLQGHQCAAVPQQPP 647
Cdd:pfam03154 445 ASHPPTSGLHQVPSQSP 461
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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